Research workbench
Human katp channel in open conformation, focused on kir (C166S G334D double mutant) and sur TMD0
Analyse Human katp channel in open conformation, focused on kir (C166S G334D double… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7S5T
- Type
- protein
- Length
- 1,284 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-sensitive inward rectifier potassium channel 11
- UniProt
- B2RC52
- Ligands
- K
- Pockets
- 16 · best druggability 0.87
Structure
electron microscopy · 1 distinct chain · 31% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | ATP-sensitive inward rectifier potassium channel 11 | protein | 321 | 31% helix, 29% strand | B2RC52 |
Ligands and binding sites
- K · Potassium ion · metal · 2 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 662 | 0.87 | 0.92 | 81 | empty |
| 2 | 231 | 0.66 | 0.84 | 42 | empty |
| 3 | 240 | 0.64 | 0.82 | 42 | empty |
| 4 | 237 | 0.63 | 0.82 | 44 | empty |
| 5 | 379 | 0.63 | 0.78 | 50 | empty |
Interfaces
6 interfaces between chains.
- B–C · 3424 Ų buried · 32 hydrogen bonds · protein-protein
- C–D · 3423 Ų buried · 33 hydrogen bonds · protein-protein
- A–D · 3421 Ų buried · 32 hydrogen bonds · protein-protein
- A–B · 3401 Ų buried · 31 hydrogen bonds · protein-protein
- A–C · 43 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 7S5T · Human KATP channel in open conformation, focused on Kir (C166S G334D double mutant) and… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt B2RC52
- Elsewhere: RCSB PDB 7S5T · PDBe 7S5T · UniProt B2RC52
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